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Volumn 386, Issue 2, 2009, Pages 427-437

Kinetics of interaction of Cotton Leaf Curl Kokhran Virus-Dabawali (CLCuKV-Dab) coat protein and its mutants with ssDNA

Author keywords

Begomoviruses; Coat protein; Cotton Leaf Curl Kokhran Virus (CLCuKV); Geminiviridae; ssDNA interaction; Surface plasmon resonance; Zinc finger motif

Indexed keywords

ALANINE; COAT PROTEIN; DNA;

EID: 62749130149     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.01.016     Document Type: Article
Times cited : (10)

References (55)
  • 1
    • 0028129204 scopus 로고
    • Whitefly transmission and efficient ssDNA accumulation of bean golden mosaic geminivirus require functional coat protein
    • Azzam O., Frazer J., de la Rosa D., Beaver J.S., Ahlquist P., and Maxwell D.P. Whitefly transmission and efficient ssDNA accumulation of bean golden mosaic geminivirus require functional coat protein. Virology 204 1 (1994) 289-296
    • (1994) Virology , vol.204 , Issue.1 , pp. 289-296
    • Azzam, O.1    Frazer, J.2    de la Rosa, D.3    Beaver, J.S.4    Ahlquist, P.5    Maxwell, D.P.6
  • 2
    • 29144528063 scopus 로고    scopus 로고
    • Silencing suppression by geminivirus proteins
    • Bisaro D.M. Silencing suppression by geminivirus proteins. Virology 344 1 (2006) 158-168
    • (2006) Virology , vol.344 , Issue.1 , pp. 158-168
    • Bisaro, D.M.1
  • 3
    • 0027373797 scopus 로고
    • Lactose repressor-operator DNA interactions: kinetic analysis by a surface plasmon resonance biosensor
    • Bondeson K., Frostell-Karlsson A., Fagerstam L., and Magnusson G. Lactose repressor-operator DNA interactions: kinetic analysis by a surface plasmon resonance biosensor. Anal. Biochem. 214 1 (1993) 245-251
    • (1993) Anal. Biochem. , vol.214 , Issue.1 , pp. 245-251
    • Bondeson, K.1    Frostell-Karlsson, A.2    Fagerstam, L.3    Magnusson, G.4
  • 5
    • 0242507588 scopus 로고    scopus 로고
    • Cotton leaf curl disease, a multicomponent begomovirus complex
    • Briddon R. Cotton leaf curl disease, a multicomponent begomovirus complex. Mol. Plant Pathol. 4 6 (2003) 427-434
    • (2003) Mol. Plant Pathol. , vol.4 , Issue.6 , pp. 427-434
    • Briddon, R.1
  • 8
    • 0028291063 scopus 로고
    • Mutations in the zinc-finger region of the yeast regulatory protein ADR1 affect both DNA binding and transcriptional activation
    • Cook W.J., Mosley S.P., Audino D.C., Mullaney D.L., Rovelli A., Stewart G., and Denis C.L. Mutations in the zinc-finger region of the yeast regulatory protein ADR1 affect both DNA binding and transcriptional activation. J. Biol. Chem. 269 12 (1994) 9374-9379
    • (1994) J. Biol. Chem. , vol.269 , Issue.12 , pp. 9374-9379
    • Cook, W.J.1    Mosley, S.P.2    Audino, D.C.3    Mullaney, D.L.4    Rovelli, A.5    Stewart, G.6    Denis, C.L.7
  • 9
    • 0031935140 scopus 로고    scopus 로고
    • Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides
    • Fisher R.J., Rein A., Fivash M., Urbaneja M.A., Casas-Finet J.R., Medaglia M., and Henderson L.E. Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides. J. Virol. 72 3 (1998) 1902-1909
    • (1998) J. Virol. , vol.72 , Issue.3 , pp. 1902-1909
    • Fisher, R.J.1    Rein, A.2    Fivash, M.3    Urbaneja, M.A.4    Casas-Finet, J.R.5    Medaglia, M.6    Henderson, L.E.7
  • 11
    • 0029943488 scopus 로고    scopus 로고
    • Optical evanescent wave methods for the study of biomolecular interactions
    • Garland P.B. Optical evanescent wave methods for the study of biomolecular interactions. Q. Rev. Biophys. 29 1 (1996) 91-117
    • (1996) Q. Rev. Biophys. , vol.29 , Issue.1 , pp. 91-117
    • Garland, P.B.1
  • 12
    • 33751000750 scopus 로고    scopus 로고
    • Differential roles of C4 and betaC1 in mediating suppression of post-transcriptional gene silencing: evidence for transactivation by the C2 of Bhendi yellow vein mosaic virus, a monopartite begomovirus
    • Gopal P., Pravin Kumar P., Sinilal B., Jose J., Kasin Yadunandam A., and Usha R. Differential roles of C4 and betaC1 in mediating suppression of post-transcriptional gene silencing: evidence for transactivation by the C2 of Bhendi yellow vein mosaic virus, a monopartite begomovirus. Virus Res. 123 1 (2007) 9-18
    • (2007) Virus Res. , vol.123 , Issue.1 , pp. 9-18
    • Gopal, P.1    Pravin Kumar, P.2    Sinilal, B.3    Jose, J.4    Kasin Yadunandam, A.5    Usha, R.6
  • 13
    • 0032127766 scopus 로고    scopus 로고
    • Alteration of zif268 zinc-finger motifs gives rise to non-native zinc-co-ordination sites but preserves wild-type DNA recognition
    • Green A., and Sarkar B. Alteration of zif268 zinc-finger motifs gives rise to non-native zinc-co-ordination sites but preserves wild-type DNA recognition. Biochem. J. 333 Pt 1 (1998) 85-90
    • (1998) Biochem. J. , vol.333 , Issue.PART 1 , pp. 85-90
    • Green, A.1    Sarkar, B.2
  • 14
    • 0034814234 scopus 로고    scopus 로고
    • Tomato yellow leaf curl virus (TYLCV) capsid protein (CP) subunit interactions: implications for viral assembly
    • Hallan V., and Gafni Y. Tomato yellow leaf curl virus (TYLCV) capsid protein (CP) subunit interactions: implications for viral assembly. Arch. Virol. 146 9 (2001) 1765-1773
    • (2001) Arch. Virol. , vol.146 , Issue.9 , pp. 1765-1773
    • Hallan, V.1    Gafni, Y.2
  • 15
    • 0018382745 scopus 로고
    • The fine structure of chloris striate mosaic virus
    • Hatta T., and Francki R.I. The fine structure of chloris striate mosaic virus. Virology 92 2 (1979) 428-435
    • (1979) Virology , vol.92 , Issue.2 , pp. 428-435
    • Hatta, T.1    Francki, R.I.2
  • 16
    • 3142777887 scopus 로고    scopus 로고
    • Interaction of DNA with the movement proteins of geminiviruses revisited
    • Hehnle S., Wege C., and Jeske H. Interaction of DNA with the movement proteins of geminiviruses revisited. J. Virol. 78 14 (2004) 7698-7706
    • (2004) J. Virol. , vol.78 , Issue.14 , pp. 7698-7706
    • Hehnle, S.1    Wege, C.2    Jeske, H.3
  • 18
    • 0343052716 scopus 로고    scopus 로고
    • Coat protein gene replacement results in whitefly transmission of an insect nontransmissible geminivirus isolate
    • Hofer P., Bedford I.D., Markham P.G., Jeske H., and Frischmuth T. Coat protein gene replacement results in whitefly transmission of an insect nontransmissible geminivirus isolate. Virology 236 2 (1997) 288-295
    • (1997) Virology , vol.236 , Issue.2 , pp. 288-295
    • Hofer, P.1    Bedford, I.D.2    Markham, P.G.3    Jeske, H.4    Frischmuth, T.5
  • 19
    • 0035841621 scopus 로고    scopus 로고
    • Exchange of three amino acids in the coat protein results in efficient whitefly transmission of a nontransmissible Abutilon mosaic virus isolate
    • Hohnle M., Hofer P., Bedford I.D., Briddon R.W., Markham P.G., and Frischmuth T. Exchange of three amino acids in the coat protein results in efficient whitefly transmission of a nontransmissible Abutilon mosaic virus isolate. Virology 290 1 (2001) 164-171
    • (2001) Virology , vol.290 , Issue.1 , pp. 164-171
    • Hohnle, M.1    Hofer, P.2    Bedford, I.D.3    Briddon, R.W.4    Markham, P.G.5    Frischmuth, T.6
  • 20
    • 0036008458 scopus 로고    scopus 로고
    • Evidence for recombination among the tomato leaf curl virus strains/species from Bangalore, India
    • Kirthi N., Maiya S.P., Murthy M.R., and Savithri H.S. Evidence for recombination among the tomato leaf curl virus strains/species from Bangalore, India. Arch. Virol. 147 2 (2002) 255-272
    • (2002) Arch. Virol. , vol.147 , Issue.2 , pp. 255-272
    • Kirthi, N.1    Maiya, S.P.2    Murthy, M.R.3    Savithri, H.S.4
  • 22
    • 0348196689 scopus 로고    scopus 로고
    • A conserved zinc finger motif in the coat protein of Tomato leaf curl Bangalore virus is responsible for binding to ssDNA
    • Kirthi N., and Savithri H.S. A conserved zinc finger motif in the coat protein of Tomato leaf curl Bangalore virus is responsible for binding to ssDNA. Arch. Virol. 148 12 (2003) 2369-2380
    • (2003) Arch. Virol. , vol.148 , Issue.12 , pp. 2369-2380
    • Kirthi, N.1    Savithri, H.S.2
  • 23
    • 0029032723 scopus 로고
    • Protein motifs 5. Zinc fingers
    • Klug A., and Schwabe J.W. Protein motifs 5. Zinc fingers. FASEB J. 9 8 (1995) 597-604
    • (1995) FASEB J. , vol.9 , Issue.8 , pp. 597-604
    • Klug, A.1    Schwabe, J.W.2
  • 24
    • 0034663134 scopus 로고    scopus 로고
    • Intracellular and intercellular movement of maize streak geminivirus V1 and V2 proteins transiently expressed as green fluorescent protein fusions
    • Kotlizky G., Boulton M.I., Pitaksutheepong C., Davies J.W., and Epel B.L. Intracellular and intercellular movement of maize streak geminivirus V1 and V2 proteins transiently expressed as green fluorescent protein fusions. Virology 274 1 (2000) 32-38
    • (2000) Virology , vol.274 , Issue.1 , pp. 32-38
    • Kotlizky, G.1    Boulton, M.I.2    Pitaksutheepong, C.3    Davies, J.W.4    Epel, B.L.5
  • 25
    • 33750416922 scopus 로고    scopus 로고
    • Protein-protein interactions and nuclear trafficking of coat protein and betaC1 protein associated with Bhendi yellow vein mosaic disease
    • Kumar P.P., Usha R., Zrachya A., Levy Y., Spanov H., and Gafni Y. Protein-protein interactions and nuclear trafficking of coat protein and betaC1 protein associated with Bhendi yellow vein mosaic disease. Virus Res. 122 1-2 (2006) 127-136
    • (2006) Virus Res. , vol.122 , Issue.1-2 , pp. 127-136
    • Kumar, P.P.1    Usha, R.2    Zrachya, A.3    Levy, Y.4    Spanov, H.5    Gafni, Y.6
  • 26
    • 0032006575 scopus 로고    scopus 로고
    • Nuclear import of the capsid protein of tomato yellow leaf curl virus (TYLCV) in plant and insect cells
    • Kunik T., Palanichelvam K., Czosnek H., Citovsky V., and Gafni Y. Nuclear import of the capsid protein of tomato yellow leaf curl virus (TYLCV) in plant and insect cells. Plant J. 13 3 (1998) 393-399
    • (1998) Plant J. , vol.13 , Issue.3 , pp. 393-399
    • Kunik, T.1    Palanichelvam, K.2    Czosnek, H.3    Citovsky, V.4    Gafni, Y.5
  • 27
    • 84907993462 scopus 로고
    • Geminivirus: genome structure and gene function
    • Lazarowitz S.G. Geminivirus: genome structure and gene function. Crit. Rev. Plant Sci. 11 (1992) 327-349
    • (1992) Crit. Rev. Plant Sci. , vol.11 , pp. 327-349
    • Lazarowitz, S.G.1
  • 28
    • 0030978731 scopus 로고    scopus 로고
    • Maize streak virus coat protein binds single- and double-stranded DNA in vitro
    • Liu H., Boulton M.I., and Davies J.W. Maize streak virus coat protein binds single- and double-stranded DNA in vitro. J. Gen. Virol. 78 Pt 6 (1997) 1265-1270
    • (1997) J. Gen. Virol. , vol.78 , Issue.PART 6 , pp. 1265-1270
    • Liu, H.1    Boulton, M.I.2    Davies, J.W.3
  • 30
    • 0031892446 scopus 로고    scopus 로고
    • Zinc fingers are sticking together
    • Mackay J.P., and Crossley M. Zinc fingers are sticking together. Trends Biochem. Sci. 23 1 (1998) 1-4
    • (1998) Trends Biochem. Sci. , vol.23 , Issue.1 , pp. 1-4
    • Mackay, J.P.1    Crossley, M.2
  • 31
    • 84990437815 scopus 로고
    • Design and chacterization of a ligand-binding metellopeptide
    • Merkle D.L., Schmidt M.H., and JM B. Design and chacterization of a ligand-binding metellopeptide. J. Am. Chem. Soc. 113 (1991) 5450-5451
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5450-5451
    • Merkle, D.L.1    Schmidt, M.H.2    JM, B.3
  • 32
    • 0034581194 scopus 로고    scopus 로고
    • Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE
    • Myszka D.G. Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE. Methods Enzymol. 323 (2000) 325-340
    • (2000) Methods Enzymol. , vol.323 , pp. 325-340
    • Myszka, D.G.1
  • 33
    • 0033119556 scopus 로고    scopus 로고
    • Instrumental biosensors: new perspectives for the analysis of biomolecular interactions
    • Nice E.C., and Catimel B. Instrumental biosensors: new perspectives for the analysis of biomolecular interactions. BioEssays 21 4 (1999) 339-352
    • (1999) BioEssays , vol.21 , Issue.4 , pp. 339-352
    • Nice, E.C.1    Catimel, B.2
  • 34
    • 0031798444 scopus 로고    scopus 로고
    • Amino acids in the capsid protein of tomato yellow leaf curl virus that are crucial for systemic infection, particle formation, and insect transmission
    • Noris E., Vaira A.M., Caciagli P., Masenga V., Gronenborn B., and Accotto G.P. Amino acids in the capsid protein of tomato yellow leaf curl virus that are crucial for systemic infection, particle formation, and insect transmission. J. Virol. 72 12 (1998) 10050-10057
    • (1998) J. Virol. , vol.72 , Issue.12 , pp. 10050-10057
    • Noris, E.1    Vaira, A.M.2    Caciagli, P.3    Masenga, V.4    Gronenborn, B.5    Accotto, G.P.6
  • 35
    • 0028157937 scopus 로고
    • Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature
    • O'Shannessy D.J. Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature. Curr. Opin. Biotechnol. 5 1 (1994) 65-71
    • (1994) Curr. Opin. Biotechnol. , vol.5 , Issue.1 , pp. 65-71
    • O'Shannessy, D.J.1
  • 36
    • 0032974246 scopus 로고    scopus 로고
    • Kinetic analysis of DNA binding by the c-Myb DNA-binding domain using surface plasmon resonance
    • Oda M., Furukawa K., Sarai A., and Nakamura H. Kinetic analysis of DNA binding by the c-Myb DNA-binding domain using surface plasmon resonance. FEBS Lett. 454 3 (1999) 288-292
    • (1999) FEBS Lett. , vol.454 , Issue.3 , pp. 288-292
    • Oda, M.1    Furukawa, K.2    Sarai, A.3    Nakamura, H.4
  • 37
    • 0030588207 scopus 로고    scopus 로고
    • The role of AV2 ("precoat") and coat protein in viral replication and movement in tomato leaf curl geminivirus
    • Padidam M., Beachy R.N., and Fauquet C.M. The role of AV2 ("precoat") and coat protein in viral replication and movement in tomato leaf curl geminivirus. Virology 224 2 (1996) 390-404
    • (1996) Virology , vol.224 , Issue.2 , pp. 390-404
    • Padidam, M.1    Beachy, R.N.2    Fauquet, C.M.3
  • 38
    • 0031793205 scopus 로고    scopus 로고
    • The capsid protein of tomato yellow leaf curl virus binds cooperatively to single-stranded DNA
    • Palanichelvam K., Kunik T., Citovsky V., and Gafni Y. The capsid protein of tomato yellow leaf curl virus binds cooperatively to single-stranded DNA. J. Gen. Virol. 79 Pt 11 (1998) 2829-2833
    • (1998) J. Gen. Virol. , vol.79 , Issue.PART 11 , pp. 2829-2833
    • Palanichelvam, K.1    Kunik, T.2    Citovsky, V.3    Gafni, Y.4
  • 40
    • 0035814503 scopus 로고    scopus 로고
    • Functional analysis of proteins involved in movement of the monopartite begomovirus, tomato yellow leaf curl virus
    • Rojas M.R., Jiang H., Salati R., Xoconostle-Cazares B., Sudarshana M.R., Lucas W.J., and Gilbertson R.L. Functional analysis of proteins involved in movement of the monopartite begomovirus, tomato yellow leaf curl virus. Virology 291 1 (2001) 110-125
    • (2001) Virology , vol.291 , Issue.1 , pp. 110-125
    • Rojas, M.R.1    Jiang, H.2    Salati, R.3    Xoconostle-Cazares, B.4    Sudarshana, M.R.5    Lucas, W.J.6    Gilbertson, R.L.7
  • 41
    • 0029881939 scopus 로고    scopus 로고
    • Transcription factor IIIA (TFIIIA) in the second decade
    • Shastry B.S. Transcription factor IIIA (TFIIIA) in the second decade. J. Cell. Sci. 109 Pt 3 (1996) 535-539
    • (1996) J. Cell. Sci. , vol.109 , Issue.PART 3 , pp. 535-539
    • Shastry, B.S.1
  • 42
    • 0031239424 scopus 로고    scopus 로고
    • Biotechnological applications of surface plasmon resonance
    • Silin, and Plant. Biotechnological applications of surface plasmon resonance. Trends Biotechnol. 15 (1997) 353-359
    • (1997) Trends Biotechnol. , vol.15 , pp. 353-359
    • Silin1    Plant2
  • 43
    • 0022423295 scopus 로고
    • Characterisation of DNA forms associated with cassava latent virus infection
    • Stanley J., and Townsend R. Characterisation of DNA forms associated with cassava latent virus infection. Nucleic Acids Res. 13 7 (1985) 2189-2206
    • (1985) Nucleic Acids Res. , vol.13 , Issue.7 , pp. 2189-2206
    • Stanley, J.1    Townsend, R.2
  • 45
    • 0026040885 scopus 로고
    • Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: residues that contact DNA and that transactivate
    • Thukral S.K., Morrison M.L., and Young E.T. Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: residues that contact DNA and that transactivate. Proc. Natl. Acad. Sci. U.S.A. 88 20 (1991) 9188-9192
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , Issue.20 , pp. 9188-9192
    • Thukral, S.K.1    Morrison, M.L.2    Young, E.T.3
  • 46
    • 0026718890 scopus 로고
    • Mutations in the zinc fingers of ADR1 that change the specificity of DNA binding and transactivation
    • Thukral S.K., Morrison M.L., and Young E.T. Mutations in the zinc fingers of ADR1 that change the specificity of DNA binding and transactivation. Mol. Cell. Biol. 12 6 (1992) 2784-2792
    • (1992) Mol. Cell. Biol. , vol.12 , Issue.6 , pp. 2784-2792
    • Thukral, S.K.1    Morrison, M.L.2    Young, E.T.3
  • 47
    • 0037081803 scopus 로고    scopus 로고
    • Kinetic study of various binding modes between human DNA polymerase beta and different DNA substrates by surface-plasmon-resonance biosensor
    • Tsoi P.Y., and Yang M. Kinetic study of various binding modes between human DNA polymerase beta and different DNA substrates by surface-plasmon-resonance biosensor. Biochem. J. 361 Pt 2 (2002) 317-325
    • (2002) Biochem. J. , vol.361 , Issue.PART 2 , pp. 317-325
    • Tsoi, P.Y.1    Yang, M.2
  • 48
    • 1242297015 scopus 로고    scopus 로고
    • Short deletions in nuclear targeting sequences of African cassava mosaic virus coat protein prevent geminivirus twinned particle formation
    • Unseld S., Frischmuth T., and Jeske H. Short deletions in nuclear targeting sequences of African cassava mosaic virus coat protein prevent geminivirus twinned particle formation. Virology 318 1 (2004) 90-101
    • (2004) Virology , vol.318 , Issue.1 , pp. 90-101
    • Unseld, S.1    Frischmuth, T.2    Jeske, H.3
  • 50
    • 0031575521 scopus 로고    scopus 로고
    • Genetic analysis of the monopartite tomato yellow leaf curl geminivirus: roles of V1, V2, and C2 ORFs in viral pathogenesis
    • Wartig L., Kheyr-Pour A., Noris E., De Kouchkovsky F., Jouanneau F., Gronenborn B., and Jupin I. Genetic analysis of the monopartite tomato yellow leaf curl geminivirus: roles of V1, V2, and C2 ORFs in viral pathogenesis. Virology 228 2 (1997) 132-140
    • (1997) Virology , vol.228 , Issue.2 , pp. 132-140
    • Wartig, L.1    Kheyr-Pour, A.2    Noris, E.3    De Kouchkovsky, F.4    Jouanneau, F.5    Gronenborn, B.6    Jupin, I.7
  • 51
    • 0032321758 scopus 로고    scopus 로고
    • Abutilon mosaic geminivirus proteins expressed and phosphorylated in Escherichia coli
    • Wege C., and Jeske H. Abutilon mosaic geminivirus proteins expressed and phosphorylated in Escherichia coli. J. Phytopathol. 146 (1998) 613-621
    • (1998) J. Phytopathol. , vol.146 , pp. 613-621
    • Wege, C.1    Jeske, H.2
  • 52
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner M.P., Costa G.L., Schoettlin W., Cline J., Mathur E., and Bauer J.C. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151 1-2 (1994) 119-123
    • (1994) Gene , vol.151 , Issue.1-2 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6
  • 53
    • 0030816177 scopus 로고    scopus 로고
    • Difference in affinity for DNA between HMG proteins 1 and 2 determined by surface plasmon resonance measurements
    • Yamamoto A., Ando Y., Yoshioka K., Saito K., Tanabe T., Shirakawa H., and Yoshida M. Difference in affinity for DNA between HMG proteins 1 and 2 determined by surface plasmon resonance measurements. J. Biochem. (Tokyo) 122 3 (1997) 586-594
    • (1997) J. Biochem. (Tokyo) , vol.122 , Issue.3 , pp. 586-594
    • Yamamoto, A.1    Ando, Y.2    Yoshioka, K.3    Saito, K.4    Tanabe, T.5    Shirakawa, H.6    Yoshida, M.7
  • 54
    • 0033547783 scopus 로고    scopus 로고
    • Differences in DNA recognition and conformational change activity between boxes A and B in HMG2 protein
    • Yoshioka K., Saito K., Tanabe T., Yamamoto A., Ando Y., Nakamura Y., Shirakawa H., and Yoshida M. Differences in DNA recognition and conformational change activity between boxes A and B in HMG2 protein. Biochemistry 38 2 (1999) 589-595
    • (1999) Biochemistry , vol.38 , Issue.2 , pp. 589-595
    • Yoshioka, K.1    Saito, K.2    Tanabe, T.3    Yamamoto, A.4    Ando, Y.5    Nakamura, Y.6    Shirakawa, H.7    Yoshida, M.8


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